An inhibitor of ALPHA-GLUCOSIDASES that retards the digestion and absorption of DIETARY CARBOHYDRATES in the SMALL INTESTINE.
Oligosaccharides containing three monosaccharide units linked by glycosidic bonds.
Enzymes that catalyze the exohydrolysis of 1,4-alpha-glucosidic linkages with release of alpha-glucose. Deficiency of alpha-1,4-glucosidase may cause GLYCOGEN STORAGE DISEASE TYPE II.
Six-carbon pyranose sugars in which the OXYGEN is replaced by a NITROGEN atom.
Substances which lower blood glucose levels.
1,4-alpha-D-Glucan-1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase/dextrin 6 alpha-D-glucanohydrolase. An enzyme system having both 4-alpha-glucanotransferase (EC and amylo-1,6-glucosidase (EC activities. As a transferase it transfers a segment of a 1,4-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or another 1,4-alpha-D-glucan. As a glucosidase it catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-1,6-glucosidase activity is deficient in glycogen storage disease type III.
Enzymes that catalyze the endohydrolysis of 1,4-alpha-glycosidic linkages in STARCH; GLYCOGEN; and related POLYSACCHARIDES and OLIGOSACCHARIDES containing 3 or more 1,4-alpha-linked D-glucose units.
Sequelae of gastrectomy from the second week after operation on. Include recurrent or anastomotic ulcer, postprandial syndromes (DUMPING SYNDROME and late postprandial hypoglycemia), disordered bowel action, and nutritional deficiencies.
Enzymes that hydrolyze O-glucosyl-compounds. (Enzyme Nomenclature, 1992) EC 3.2.1.-.
An enzyme that catalyzes the hydrolysis of terminal 1,4-linked alpha-D-glucose residues successively from non-reducing ends of polysaccharide chains with the release of beta-glucose. It is also able to hydrolyze 1,6-alpha-glucosidic bonds when the next bond in sequence is 1,4.
A family of gram-positive, saprophytic bacteria occurring in soil and aquatic environments.
A dextrodisaccharide from malt and starch. It is used as a sweetening agent and fermentable intermediate in brewing. (Grant & Hackh's Chemical Dictionary, 5th ed)
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
Production or presence of gas in the gastrointestinal tract which may be expelled through the anus.

Manganese sulfate-dependent glycosylation of endogenous glycoproteins in human skeletal muscle is catalyzed by a nonglucose 6-P-dependent glycogen synthase and not glycogenin. (1/145)

Glycogenin, a Mn2+-dependent, self-glucosylating protein, is considered to catalyze the initial glucosyl transfer steps in glycogen biogenesis. To study the physiologic significance of this enzyme, measurements of glycogenin mediated glucose transfer to endogenous trichloroacetic acid precipitable material (protein-bound glycogen, i.e., glycoproteins) in human skeletal muscle were attempted. Although glycogenin protein was detected in muscle extracts, activity was not, even after exercise that resulted in marked glycogen depletion. Instead, a MnSO4-dependent glucose transfer to glycoproteins, inhibited by glycogen and UDP-pyridoxal (which do not affect glycogenin), and unaffected by CDP (a potent inhibitor of glycogenin), was consistently detected. MnSO4-dependent activity increased in concert with glycogen synthase fractional activity after prolonged exercise, and the MnSO4-dependent enzyme stimulated glucosylation of glycoproteins with molecular masses lower than those glucosylated by glucose 6-P-dependent glycogen synthase. Addition of purified glucose 6-P-dependent glycogen synthase to the muscle extract did not affect MnSO4-dependent glucose transfer, whereas glycogen synthase antibody completely abolished MnSO4-dependent activity. It is concluded that: (1) MnSO4-dependent glucose transfer to glycoproteins is catalyzed by a nonglucose 6-P-dependent form of glycogen synthase; (2) MnSO4-dependent glycogen synthase has a greater affinity for low molecular mass glycoproteins and may thus play a more important role than glucose 6-P-dependent glycogen synthase in the initial stages of glycogen biogenesis; and (3) glycogenin is generally inactive in human muscle in vivo.  (+info)

Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain. (2/145)

A maltogenic amylase gene was cloned in Escherichia coli from a gram-negative thermophilic bacterium, Thermus strain IM6501. The gene encoded an enzyme (ThMA) with a molecular mass of 68 kDa which was expressed by the expression vector p6xHis119. The optimal temperature of ThMA was 60 degrees C, which was higher than those of other maltogenic amylases reported so far. Thermal inactivation kinetic analysis of ThMA indicated that it was stabilized in the presence of 10 mM EDTA. ThMA harbored both hydrolysis and transglycosylation activities. It hydrolyzed beta-cyclodextrin and starch mainly to maltose and pullulan to panose. ThMA not only hydrolyzed acarbose, an amylase inhibitor, to glucose and pseudotrisaccharide (PTS) but also transferred PTS to 17 sugar acceptors, including glucose, fructose, maltose, cellobiose, etc. Structural analysis of acarbose transfer products by using methylation, thin-layer chromatography, high-performance ion chromatography, and nuclear magnetic resonance indicated that PTS was transferred primarily to the C-6 of the acceptors and at lower degrees to the C-3 and/or C-4. The transglycosylation of sugar to methyl-alpha-D-glucopyranoside by forming an alpha-(1,3)-glycosidic linkage was demonstrated for the first time by using acarbose and ThMA. Kinetic analysis of the acarbose transfer products showed that the C-4 transfer product formed most rapidly but readily hydrolyzed, while the C-6 transfer product was stable and accumulated in the reaction mixture as the main product.  (+info)

The AcbC protein from Actinoplanes species is a C7-cyclitol synthase related to 3-dehydroquinate synthases and is involved in the biosynthesis of the alpha-glucosidase inhibitor acarbose. (3/145)

The putative biosynthetic gene cluster for the alpha-glucosidase inhibitor acarbose was identified in the producer Actinoplanes sp. 50/110 by cloning a DNA segment containing the conserved gene for dTDP-D-glucose 4,6-dehydratase, acbB. The two flanking genes were acbA (dTDP-D-glucose synthase) and acbC, encoding a protein with significant similarity to 3-dehydroquinate synthases (AroB proteins). The acbC gene was overexpressed heterologously in Streptomyces lividans 66, and the product was shown to be a C7-cyclitol synthase using sedo-heptulose 7-phosphate, but not ido-heptulose 7-phosphate, as its substrate. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety of acarbose. A possible five-step reaction mechanism is proposed for the cyclization reaction catalyzed by AcbC based on the recent analysis of the three-dimensional structure of a eukaryotic 3-dehydroquinate synthase domain (Carpenter, E. P., Hawkins, A. R., Frost, J. W., and Brown, K. A. (1998) Nature 394, 299-302).  (+info)

Acarbose, a pseudooligosaccharide, is transported but not metabolized by the maltose-maltodextrin system of Escherichia coli. (4/145)

The pseudooligosaccharide acarbose is a potent inhibitor of amylases, glucosidases, and cyclodextrin glycosyltransferase and is clinically used for the treatment of so-called type II or insulin-independent diabetes. The compound consists of an unsaturated aminocyclitol, a deoxyhexose, and a maltose. The unsaturated aminocyclitol moiety (also called valienamine) is primarily responsible for the inhibition of glucosidases. Due to its structural similarity to maltotetraose, we have investigated whether acarbose is recognized as a substrate by the maltose/maltodextrin system of Escherichia coli. Acarbose at millimolar concentrations specifically affected the growth of E. coli K-12 on maltose as the sole source of carbon and energy. Uptake of radiolabeled maltose was competitively inhibited by acarbose, with a Ki of 1.1 microM. Maltose-grown cells transported radiolabeled acarbose, indicating that the compound is recognized as a substrate. Studying the interaction of acarbose with purified maltoporin in black lipid membranes revealed that the kinetics of acarbose binding to LamB is asymmetric. The on-rate of acarbose is approximately 30 times lower when the molecule enters the pore from the extracellular side than when it enters from the periplasmic side. Acarbose could not be utilized as a carbon source since the compound alone was not a substrate of amylomaltase (MalQ) and was only poorly attacked by maltodextrin glucosidase (MalZ).  (+info)

A randomized double-blind trial of acarbose in type 2 diabetes shows improved glycemic control over 3 years (U.K. Prospective Diabetes Study 44) (5/145)

OBJECTIVE: To determine the degree to which alpha-glucosidase inhibitors, with their unique mode of action primarily reducing postprandial hyperglycemia, offer an additional therapeutic approach in the long-term treatment of type 2 diabetes. RESEARCH DESIGN AND METHODS: We studied 1,946 patients (63% men) who were previously enrolled in the U.K. Prospective Diabetes Study (UKPDS). The patients were randomized to acarbose (n = 973), titrating to a maximum dose of 100 mg three times per day, or to matching placebo (n = 973). Mean +/- SD age was 59 +/- 9 years, body weight 84 +/- 17 kg, diabetes duration 7.6 +/- 2.9 years, median (interquartile range) HbA1c 7.9% (6.7-9.5), and fasting plasma glucose (FPG) 8.7 mmol/l (6.8-11.1). Fourteen percent of patients were treated with diet alone, 52% with monotherapy, and 34% with combined therapy. Patients were monitored in UKPDS clinics every 4 months for 3 years. The main outcome measures were HbA1c, FPG, body weight, compliance with study medication, incidence of side effects, and frequency of major clinical events. RESULTS: At 3 years, a lower proportion of patients were taking acarbose compared with placebo (39 vs. 58%, P < 0.0001), the main reasons for noncompliance being flatulence (30 vs. 12%, P < 0.0001) and diarrhea (16 vs. 8%, P < 0.05). Analysis by intention to treat showed that patients allocated to acarbose, compared with placebo, had 0.2% significantly lower median HbA1c at 3 years (P < 0.001). In patients remaining on their allocated therapy, the HbA1c difference at 3 years (309 acarbose, 470 placebo) was 0.5% lower median HbA1c (8.1 vs. 8.6%, P < 0.0001). Acarbose appeared to be equally efficacious when given in addition to diet alone; in addition to monotherapy with a sulfonylurea, metformin, or insulin; or in combination with more complex treatment regimens. No significant differences were seen in FPG, body weight, incidence of hypoglycemia, or frequency of major clinical events. CONCLUSIONS: Acarbose significantly improved glycemic control over 3 years in patients with established type 2 diabetes, irrespective of concomitant therapy for diabetes. Careful titration of acarbose is needed in view of the increased noncompliance rate seen secondary to the known side effects.  (+info)

Changes of fermentation pathways of fecal microbial communities associated with a drug treatment that increases dietary starch in the human colon. (6/145)

Acarbose inhibits starch digestion in the human small intestine. This increases the amount of starch available for microbial fermentation to acetate, propionate, and butyrate in the colon. Relatively large amounts of butyrate are produced from starch by colonic microbes. Colonic epithelial cells use butyrate as an energy source, and butyrate causes the differentiation of colon cancer cells. In this study we investigated whether colonic fermentation pathways changed during treatment with acarbose. We examined fermentations by fecal suspensions obtained from subjects who participated in an acarbose-placebo crossover trial. After incubation with [1-13C]glucose and 12CO2 or with unlabeled glucose and 13CO2, the distribution of 13C in product C atoms was determined by nuclear magnetic resonance spectrometry and gas chromatography-mass spectrometry. Regardless of the treatment, acetate, propionate, and butyrate were produced from pyruvate formed by the Embden-Meyerhof-Parnas pathway. Considerable amounts of acetate were also formed by the reduction of CO2. Butyrate formation from glucose increased and propionate formation decreased with acarbose treatment. Concomitantly, the amounts of CO2 reduced to acetate were 30% of the total acetate in untreated subjects and 17% of the total acetate in the treated subjects. The acetate, propionate, and butyrate concentrations were 57, 20, and 23% of the total final concentrations, respectively, for the untreated subjects and 57, 13, and 30% of the total final concentrations, respectively, for the treated subjects.  (+info)

Structure-function relationships in glucoamylases encoded by variant Saccharomycopsis fibuligera genes. (7/145)

The mutation Gly467-->Ser in Glu glucoamylase was designed to investigate differences between two highly homologous wild-type Saccharomycopsis fibuligera Gla and Glu glucoamylases. Gly467, localized in the conserved active site region, S5, is replaced by Ser in the Gla glucoamylase. These amino acid residues are the only two known to occupy this position in the elucidated glucoamylase sequences. The data from the kinetic analysis revealed that replacement of Gly467 with Ser in Glu glucoamylase decreased the kcat towards all substrates tested to values comparable with those of the Gla enzyme. Moreover, the mutant glucoamylase appeared to be less stable compared to the wild-type Glu glucoamylase with respect to thermal unfolding. Microcalorimetric titration studies of the interaction with the inhibitor acarbose indicated differences in the binding between Gla and Glu enzymes. The Gla glucoamylase, although less active, binds acarbose stronger (Ka congruent with 10(13).M(-1)) than the Glu enzyme (Ka congruent with 10(12).M(-1)). In all enzymes studied, the binding of acarbose was clearly driven by enthalpy, with a slightly favorable entropic contribution. The binding of another glucoamylase inhibitor, 1-deoxynojirimycin, was about 8-9 orders of magnitude weaker (Ka congruent with 10(4).M(-1)) than that of acarbose. From comparison of kinetic parameters for the nonglycosylated and glycosylated enzymes it can be deduced that the glycosylation does not play a critical role in enzymatic activity. However, results from differential scanning calorimetry demonstrate an important role of the carbohydrate moiety in the thermal stability of glucoamylase.  (+info)

Mechanism of porcine pancreatic alpha-amylase inhibition of amylose and maltopentaose hydrolysis by kidney bean (Phaseolus vulgaris) inhibitor and comparison with that by acarbose. (8/145)

The effects of Phaseolus vulgaris inhibitor (alpha-AI) on the amylose and maltopentaose hydrolysis catalysed by porcine pancreatic alpha-amylase (PPA) were investigated. Based on a statistical analysis of the kinetic data and using the general velocity equation, which is valid at equilibrium for all types of inhibition in a single-substrate reaction, it was concluded that the inhibitory mode is of the mixed noncompetitive type involving two molecules of inhibitor. In line with this conclusion, the Lineweaver-Burk primary plots intersect in the second quadrant and the secondary plots of the slopes and the intercepts versus the inhibitor concentrations are parabolic curves, whether the substrate used was amylose or maltopentaose. A specific inhibition model of the mixed noncompetitive type applies here. This model differs from those previously proposed for acarbose [Al Kazaz, M., Desseaux, V., Marchis-Mouren, G., Payan, F., Forest, E. & Santimone, M. (1996) Eur. J. Biochem. 241, 787-796 and Al Kazaz, M., Desseaux, V., Marchis-Mouren, G., Prodanov, E. & Santimone, M. (1998) Eur. J. Biochem. 252, 100-107]. In particular, with alpha-AI, the inhibition takes place only when PPA and alpha-AI are preincubated together before the substrate is added. This shows that the inhibitory PPA-alphaAI complex is formed during the preincubation period. Secondly, other inhibitory complexes are formed, in which two molecules of inhibitor are bound to either the free enzyme or the enzyme-substrate complex. The catalytic efficiency was determined both with and without inhibitor. Using the same molar concentration of inhibitor, alpha-AI was found to be a much stronger inhibitor than acarbose. However, when the inhibitor amount is expressed on a weight basis (mg x L-1), the opposite conclusion is drawn. In addition, limited proteolysis was performed on PPA alone and on the alpha-AI-PPA complex. The results show that, in the complex, PPA is more sensitive to subtilisin attack, and shorter fragments are obtained. These data reflect the conformational changes undergone by PPA as the result of the protein inhibitor binding, which differ from those previously observed with acarbose.  (+info)

Acarbose is a medication that belongs to a class of drugs called alpha-glucosidase inhibitors. It is used in the management of type 2 diabetes mellitus. Acarbose works by slowing down the digestion of carbohydrates in the small intestine, which helps to prevent spikes in blood sugar levels after meals.

By blocking the enzyme alpha-glucosidase, acarbose prevents the breakdown of complex carbohydrates into simple sugars, such as glucose, in the small intestine. This results in a slower and more gradual absorption of glucose into the bloodstream, which helps to prevent postprandial hyperglycemia (high blood sugar levels after meals).

Acarbose is typically taken orally three times a day, before meals containing carbohydrates. Common side effects include gastrointestinal symptoms such as bloating, flatulence, and diarrhea. It is important to note that acarbose should be used in conjunction with a healthy diet and regular exercise to effectively manage blood sugar levels in individuals with type 2 diabetes.

A trisaccharide is a type of carbohydrate molecule composed of three monosaccharide units joined together by glycosidic bonds. Monosaccharides are simple sugars, such as glucose, fructose, and galactose, which serve as the building blocks of more complex carbohydrates.

In a trisaccharide, two monosaccharides are linked through a glycosidic bond to form a disaccharide, and then another monosaccharide is attached to the disaccharide via another glycosidic bond. The formation of these bonds involves the loss of a water molecule (dehydration synthesis) between the hemiacetal or hemiketal group of one monosaccharide and the hydroxyl group of another.

Examples of trisaccharides include raffinose (glucose + fructose + galactose), maltotriose (glucose + glucose + glucose), and melezitose (glucose + fructose + glucose). Trisaccharides can be found naturally in various foods, such as honey, sugar beets, and some fruits and vegetables. They play a role in energy metabolism, serving as an energy source for the body upon digestion into monosaccharides, which are then absorbed into the bloodstream and transported to cells for energy production or storage.

Alpha-glucosidases are a group of enzymes that break down complex carbohydrates into simpler sugars, such as glucose, by hydrolyzing the alpha-1,4 and alpha-1,6 glycosidic bonds in oligosaccharides, disaccharides, and polysaccharides. These enzymes are located on the brush border of the small intestine and play a crucial role in carbohydrate digestion and absorption.

Inhibitors of alpha-glucosidases, such as acarbose and miglitol, are used in the treatment of type 2 diabetes to slow down the digestion and absorption of carbohydrates, which helps to reduce postprandial glucose levels and improve glycemic control.

Imino pyranoses are not a recognized medical term or concept. However, in the field of chemistry, imino pyranoses refer to a class of compounds that are derived from pyranose sugars through a chemical reaction known as the Amadori rearrangement. In this reaction, the carbonyl group (aldehyde or ketone) of a reducing sugar reacts with an amine to form a new compound with a carbon-nitrogen double bond (imine).

In the case of pyranose sugars, which are cyclic forms of monosaccharides with six members in the ring, the Amadori rearrangement leads to the formation of imino pyranoses. These compounds can undergo further reactions and modifications, leading to a variety of chemical structures that have been studied for their potential biological activity.

Therefore, while not directly related to medical definitions, imino pyranoses are an area of interest in biochemistry and may have implications for understanding the chemistry of certain biological processes or developing new therapeutic agents.

Hypoglycemic agents are a class of medications that are used to lower blood glucose levels in the treatment of diabetes mellitus. These medications work by increasing insulin sensitivity, stimulating insulin release from the pancreas, or inhibiting glucose production in the liver. Examples of hypoglycemic agents include sulfonylureas, meglitinides, biguanides, thiazolidinediones, DPP-4 inhibitors, SGLT2 inhibitors, and GLP-1 receptor agonists. It's important to note that the term "hypoglycemic" refers to a condition of abnormally low blood glucose levels, but in this context, the term is used to describe agents that are used to treat high blood glucose levels (hyperglycemia) associated with diabetes.

The Glycogen Debranching Enzyme System, also known as glycogen debranching enzyme or Amy-1, is a crucial enzyme complex in human biochemistry. It plays an essential role in the metabolism of glycogen, which is a large, branched polymer of glucose that serves as the primary form of energy storage in animals and fungi.

The Glycogen Debranching Enzyme System consists of two enzymatic activities: a transferase and an exo-glucosidase. The transferase activity transfers a segment of a branched glucose chain to another part of the same or another glycogen molecule, while the exo-glucosidase activity cleaves the remaining single glucose units from the outer branches of the glycogen molecule.

This enzyme system is responsible for removing the branched structures of glycogen, allowing the linear chains to be further degraded by other enzymes into glucose molecules that can be used for energy production or stored for later use. Defects in this enzyme complex can lead to several genetic disorders, such as Glycogen Storage Disease Type III (Cori's disease) and Type IV (Andersen's disease), which are characterized by the accumulation of abnormal glycogen molecules in various tissues.

Alpha-amylases are a type of enzyme that breaks down complex carbohydrates, such as starch and glycogen, into simpler sugars like maltose, maltotriose, and glucose. These enzymes catalyze the hydrolysis of alpha-1,4 glycosidic bonds in these complex carbohydrates, making them more easily digestible.

Alpha-amylases are produced by various organisms, including humans, animals, plants, and microorganisms such as bacteria and fungi. In humans, alpha-amylases are primarily produced by the salivary glands and pancreas, and they play an essential role in the digestion of dietary carbohydrates.

Deficiency or malfunction of alpha-amylases can lead to various medical conditions, such as diabetes, kidney disease, and genetic disorders like congenital sucrase-isomaltase deficiency. On the other hand, excessive production of alpha-amylases can contribute to dental caries and other oral health issues.

Postgastrectomy syndromes refer to a group of clinical manifestations that can occur as complications or sequelae following a gastrectomy, which is the surgical removal of all or part of the stomach. These syndromes are relatively common and can have a significant impact on the patient's quality of life.

There are several types of postgastrectomy syndromes, including:

1. Dumping syndrome: This occurs when the remaining portion of the stomach is unable to adequately regulate the passage of food into the small intestine, leading to symptoms such as nausea, vomiting, abdominal cramps, diarrhea, dizziness, and sweating.
2. Gastroparesis: This is a condition where the stomach is unable to empty properly due to decreased motility, leading to symptoms such as bloating, nausea, vomiting, and early satiety.
3. Nutritional deficiencies: Following gastrectomy, there can be malabsorption of certain nutrients, including vitamin B12, iron, calcium, and folate, leading to anemia, osteoporosis, and other health problems.
4. Afferent loop syndrome: This is a rare complication that occurs when the afferent loop, which carries digestive enzymes from the pancreas and bile from the liver to the small intestine, becomes obstructed or narrowed, leading to symptoms such as abdominal pain, nausea, vomiting, and jaundice.
5. Alkaline reflux gastritis: This occurs when the alkaline contents of the small intestine reflux into the remnant stomach, causing inflammation and ulceration.
6. Bile reflux: This is a condition where bile from the small intestine flows back into the stomach, leading to symptoms such as abdominal pain, nausea, vomiting, and heartburn.

Treatment of postgastrectomy syndromes depends on the specific type and severity of the syndrome, and may include dietary modifications, medication, or surgical intervention.

Glucosidases are a group of enzymes that catalyze the hydrolysis of glycosidic bonds, specifically at the non-reducing end of an oligo- or poly saccharide, releasing a single sugar molecule, such as glucose. They play important roles in various biological processes, including digestion of carbohydrates and the breakdown of complex glycans in glycoproteins and glycolipids.

In the context of digestion, glucosidases are produced by the pancreas and intestinal brush border cells to help break down dietary polysaccharides (e.g., starch) into monosaccharides (glucose), which can then be absorbed by the body for energy production or storage.

There are several types of glucosidases, including:

1. α-Glucosidase: This enzyme is responsible for cleaving α-(1→4) and α-(1→6) glycosidic bonds in oligosaccharides and disaccharides, such as maltose, maltotriose, and isomaltose.
2. β-Glucosidase: This enzyme hydrolyzes β-(1→4) glycosidic bonds in cellobiose and other oligosaccharides derived from plant cell walls.
3. Lactase (β-Galactosidase): Although not a glucosidase itself, lactase is often included in this group because it hydrolyzes the β-(1→4) glycosidic bond between glucose and galactose in lactose, yielding free glucose and galactose.

Deficiencies or inhibition of these enzymes can lead to various medical conditions, such as congenital sucrase-isomaltase deficiency (an α-glucosidase deficiency), lactose intolerance (a lactase deficiency), and Gaucher's disease (a β-glucocerebrosidase deficiency).

Glucan 1,4-alpha-glucosidase, also known as amyloglucosidase or glucoamylase, is an enzyme that catalyzes the hydrolysis of 1,4-glycosidic bonds in starch and other oligo- and polysaccharides, breaking them down into individual glucose molecules. This enzyme specifically acts on the alpha (1->4) linkages found in amylose and amylopectin, two major components of starch. It is widely used in various industrial applications, including the production of high fructose corn syrup, alcoholic beverages, and as a digestive aid in some medical supplements.

Micromonosporaceae is a family of actinobacteria that are gram-positive, aerobic, and have high guanine-cytosine content in their DNA. These bacteria are typically found in soil and aquatic environments. They are known for producing a wide range of bioactive compounds with potential applications in medicine, agriculture, and industry. The cells of Micromonosporaceae are usually rod-shaped and may form branching filaments or remain as single cells. Some members of this family can form spores, which are often resistant to heat, drying, and chemicals.

It's worth noting that the medical significance of Micromonosporaceae is not well established, but some species have been found to produce antibiotics and other bioactive compounds with potential therapeutic applications. For example, the genus Micromonospora includes several species that are known to produce various antibiotics, such as micromonosporin, xanthomycin, and gentamicin C1A. However, further research is needed to fully understand the medical relevance of this family of bacteria.

Maltose is a disaccharide made up of two glucose molecules joined by an alpha-1,4 glycosidic bond. It is commonly found in malted barley and is created during the germination process when amylase breaks down starches into simpler sugars. Maltose is less sweet than sucrose (table sugar) and is broken down into glucose by the enzyme maltase during digestion.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

Flatulence is the medical term for the release of intestinal gas from the rectum, commonly known as passing gas or farting. It is a normal bodily function that occurs when the body digests food in the stomach and intestines.

During digestion, the body breaks down food into nutrients that can be absorbed into the bloodstream. However, not all food particles can be fully broken down, and some of them reach the large intestine, where they are fermented by bacteria. This fermentation process produces gases such as nitrogen, oxygen, carbon dioxide, hydrogen, and methane.

The buildup of these gases in the digestive tract can cause discomfort, bloating, and the urge to pass gas. The average person passes gas about 10-20 times a day, although this can vary widely from person to person.

While flatulence is a normal bodily function, excessive or frequent passing of gas can be a sign of an underlying digestive issue such as irritable bowel syndrome (IBS), lactose intolerance, or gastrointestinal infections. If you are experiencing persistent or severe symptoms, it is recommended to consult with a healthcare professional for further evaluation and treatment.

In nature, acarbose is synthesized by soil bacteria Actinoplanes sp through its precursor valienamine. And acarbose is also ... The microbiome-derived acarbose kinases are also specific to phosphorylate and inactivate acarbose. The molecular modeling ... "Acarbose". MedlinePlus Drug Information. "Acarbose: hepatitis: France, Spain". WHO Pharmaceuticals Newsletter. 1999. Archived ... acarbose was shown to extend the lifespan of female mice by 5% and of male mice by 22%. Acarbose degradation is the unique ...
Redirects to acarbose. Glucohexal (Hexal Australia) [Au]. Redirects to metformin. Glucophage (Sanofi) glucosamine (INN) ...
Precef preclamol (INN) Precose (Bayer AG). Redirects to acarbose. Pred-G Pred Predair Predamide prednazate (INN) prednazoline ( ...
"acarbose - oral, Precose". MedicineNet. Archived from the original on 1 February 2014. Retrieved 27 January 2014. "Peptimmune ... A similar medication designed for patients with Type 2 diabetes is Acarbose; which partially blocks absorption of carbohydrates ...
Miglitol is fairly well absorbed by the body, as opposed to acarbose. Moreover, acarbose inhibits pancreatic alpha-amylase in ... there are subtle differences between acarbose and miglitol. Acarbose is an oligosaccharide, whereas miglitol resembles a ... Kim TJ, Kim MJ, Kim BC, Kim JC, Cheong TK, Kim JW, Park KH (April 1999). "Modes of action of acarbose hydrolysis and ... Acarbose also blocks pancreatic alpha-amylase in addition to inhibiting membrane-bound alpha-glucosidases. Pancreatic alpha- ...
June 2002). "Biosynthesis of the C(7)-cyclitol moiety of acarbose in Actinoplanes species SE50/110. 7-O-phosphorylation of the ... Valienamine is a C-7 aminocyclitol found as a substructure of pseudooligosaccharides such as the antidiabetic drug acarbose and ... Laube, Heiner (March 2002). "Acarbose An Update of Its Therapeutic Use in Diabetes Treatment". Clinical Drug Investigation. 22 ...
Acarbose is an enzyme inhibitor that is used as a drug against type 2 diabetes. Miglustat is an iminosugar in which the ring ... Tamiflu is an enzyme inhibitor that blocks the action of influenza virus neuraminidases (sialidases). Acarbose is a ...
Laube, Heiner (March 2002). "Acarbose An Update of Its Therapeutic Use in Diabetes Treatment". Clinical Drug Investigation. 22 ... a precursor to the antidiabetic drug acarbose and to the antibiotic validamycin), teicoplanin, and ramoplanin. Actinoplanes ...
Another study indicates it may interfere with the diabetic medication acarbose. Beano was developed in 1990 by Alan Kligerman ... Lettieri JT, Dain B (1998). "Effects of beano on the tolerability and pharmacodynamics of acarbose". Clin Ther. 20 (3): 497-504 ...
The cyclomaltodextrinase is capable of degradation of acarbose to glucose and acarviosine-glucose. As of late 2007, two ... The enzyme participates in starch and sucrose metabolism and acarbose degradation. ... "Functional expression and enzymatic characterization of Lactobacillus plantarum cyclomaltodextrinase catalyzing novel acarbose ...
Acarbose may be able to prevent the development of diabetic symptoms. Hence, α-glucosidase inhibitors (like acarbose) are used ... Diabetes: Acarbose, an α-glucosidase inhibitor, competitively and reversibly inhibits α-glucosidase in the intestines. This ...
In contrast to acarbose (another alpha-glucosidase inhibitor), miglitol is systemically absorbed; however, it is not ...
... is part of the potent α-amylase inhibitor acarbose and its derivatives. Acarviosin is a product of the degradation ... of acarbose by gut microbiota, the glycoside hydrolase from gut bacteria Lactobacillus plantarum is able to hydrolyze acarbose ... "Functional expression and enzymatic characterization of Lactobacillus plantarum cyclomaltodextrinase catalyzing novel acarbose ...
The 3D structure of the pseudo-tetrasaccharide acarbose complexed with glucoamylase II(471) from Aspergillus awamori var. X100 ... Aleshin AE, Firsov LM, Honzatko RB (June 1994). "Refined structure for the complex of acarbose with glucoamylase from ...
Kim TJ, Kim MJ, Kim BC, Kim JC, Cheong TK, Kim JW, Park KH (April 1999). "Modes of action of acarbose hydrolysis and ... and Geobacillus thermoleovorans are able to degrade acarbose to glucose and acarviosine-glucose. Diderichsen B, Christiansen L ... "Molecular and enzymatic characterization of a maltogenic amylase that hydrolyzes and transglycosylates acarbose". European ...
Within the -1 subsite, isomaltose's non-reducing glucose ring was aligned to that of acarbose. Not only has the structure of ...
Metformin and acarbose help prevent the development of prediabetes, and also have a good safety profile. Evidence also supports ...
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Alpha-glucosidases are targeted by alpha-glucosidase inhibitors such as acarbose and miglitol to control diabetes mellitus type ...
Tuğrul S, Kutlu T, Pekin O, Bağlam E, Kiyak H, Oral O (October 2008). "Clinical, endocrine, and metabolic effects of acarbose, ...
"Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with acarbose and cyclodextrins demonstrate the multiple ...
There are three major drugs which belong to this class, acarbose, miglitol and voglibose, of which voglibose is the newest. A ...
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Inhibitors that are in clinical use include the anti-diabetic drugs acarbose and miglitol, and the antiviral drugs oseltamivir ...
Typical reductions in glycated hemoglobin (A1C) values are 0.5-1.0%. miglitol acarbose voglibose These medications are rarely ... Acarbose Meglitinides - nateglinide Combination of sulfonylureas plus metformin - known by generic names of the two drugs No ...
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sedoheptulose 7-phosphate derived C7N aminocyclitol natural products This class includes acarbose, validamycin, validoxylamine ... such as acarbose, validamycin A, salbostatin, cetoniacytone A, and pyralomicin 1a. 2-epi-5-epi-valiolone synthase (EEVS), one ... "Biosynthesis of the C7-cyclitol Moiety of Acarbose inActinoplanes Species SE50/110 7-O-PHOSPHORYLATION OF THE INITIAL CYCLITOL ... Synthase Related to 3-Dehydroquinate Synthases and Is Involved in the Biosynthesis of the α-Glucosidase Inhibitor Acarbose". ...
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In nature, acarbose is synthesized by soil bacteria Actinoplanes sp through its precursor valienamine. And acarbose is also ... The microbiome-derived acarbose kinases are also specific to phosphorylate and inactivate acarbose. The molecular modeling ... "Acarbose". MedlinePlus Drug Information. "Acarbose: hepatitis: France, Spain". WHO Pharmaceuticals Newsletter. 1999. Archived ... acarbose was shown to extend the lifespan of female mice by 5% and of male mice by 22%. Acarbose degradation is the unique ...
Acarbose: learn about side effects, dosage, special precautions, and more on MedlinePlus ... Before taking acarbose,. *tell your doctor and pharmacist if you are allergic to acarbose or any other drugs. ... Continue to take acarbose even if you feel well. Do not stop taking acarbose without talking to your doctor. ... Acarbose comes as a tablet to take by mouth. It is usually taken three times a day. It is very important to take each dose with ...
Davis C. Acarbose. Drug Summary. 2015 Full text (in our servers) *AEMPS. Acarbosa. Ficha técnica. 2009 Full text (in our ... Acarbose belongs to this group or family:. *ATC A10BF: Blood glucose lowering drug (Anti-diabetic). Alpha glucosidase inhibitor ... Ahr HJ, Boberg M, Krause HP, Maul W, Müller FO, Ploschke HJ, Weber H, Wünsche C. Pharmacokinetics of acarbose. Part I: ... Ahr HJ, Krause HP, Siefert HM, Steinke W, Weber H. Pharmacokinetics of acarbose. Part II: Distribution to and elimination from ...
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Although maltose is an important building block of acarbose, the maltose/maltodextrin metabolism has not been studied in ... Although maltose is an important building block of acarbose, the maltose/maltodextrin metabolism has not been studied in ... SE50/110 is the wild type of industrial production strains of the fine-chemical acarbose (acarviosyl-maltose), which is used as ... SE50/110 is the wild type of industrial production strains of the fine-chemical acarbose (acarviosyl-maltose), which is used as ...
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CH$NAME: Acarbose. CH$COMPOUND_CLASS: Carbohydrates. CH$FORMULA: C25H43NO18. CH$EXACT_MASS: 645.6174. CH$SMILES: C[C@H]1OC(OC2[ ... RECORD_TITLE: Acarbose; LC-ESI-QQQ; MS; [M+H]+. DATE: 2018.04.04. AUTHORS: Nogawa T, Okano A, CSRS, RIKEN. LICENSE: CC BY. ... Acarbose with the InChIKey XUFXOAAUWZOOIT-GPNAOJRPSA-N. ...
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Acarbose is a type of a drug that control glucose levels of your body and helps to treat diabetes. Find more at Curecrowd. ... Acarbose. Also Known As: Acarbose, Precose, Prandase. Acarbose is an anti-diabetic drug used to treat type 2 diabetes mellitus ... Since acarbose prevents the digestion of complex carbohydrates, the drug should be taken at the start of main meals (taken with ... Acarbose inhibits enzymes (glycoside hydrolases) needed to digest carbohydrates, specifically, alpha-glucosidase enzymes in the ...
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  • Take acarbose exactly as directed. (
  • Continue to take acarbose even if you feel well. (
  • Take Acarbose with the first bite of a main meal, unless your doctor tells you otherwise. (
  • Avoid taking a digestive enzyme such as pancreatin, amylase, or lipase at the same time you take acarbose. (
  • The combination of acarbose with metformin results in greater reductions of HbA1c, fasting blood glucose and post-prandial glucose than either agent alone. (
  • Because its mechanism of action is different, the effect of acarbose to enhance glycemic control is additive to that of sulfonylureas, insulin or metformin when used in combination. (
  • Is there a role for metformin or acarbose as a weight-loss agent in the absence of diabetes? (
  • Does the Addition of Acarbose to Metformin Lower HbA1c? (
  • Our study aims to investigate the in-vitro α -glucosidase inhibitory activity of Syzygium aromaticum and its herb-drug interaction with Acarbose and Metformin. (
  • The release efficiency of the microencapsulated extract was investigated and compared against microencapsulated extract and drugs (Acarbose and Metformin). (
  • IC 50 values for herb-drug interaction involving clove and Acarbose was 72.284 µg/ml and for clove and Metformin was 76.713 µg/ml, thereby displaying a herb-drug interaction. (
  • In combination with Acarbose or Metformin, it enhances the inhibition even more. (
  • 14. Effects of acarbose versus glibenclamide on glycemic excursion and oxidative stress in type 2 diabetic patients inadequately controlled by metformin: a 24-week, randomized, open-label, parallel-group comparison. (
  • After admission, the patient was found to have type 2 diabetes mellitus, for which acarbose and metformin were prescribed. (
  • When used in combination with insulin or other medications used to treat diabetes, acarbose may cause excessive lowering of blood sugar levels. (
  • In subjects with impaired glucose tolerance, acarbose increases insulin sensitivity up to 30%, suggesting that the drug may have a preventive role in the progressive transition to overt type 2 diabetes. (
  • In contrast to sulfonylureas, acarbose does not enhance insulin secretion. (
  • The current indications for acarbose are for management of glycemic control in type 2 diabetes used in combination with diet and exercise, with or without other oral hypoglycemic agents or insulin. (
  • Acarbose is sometimes used in combination with insulin or other diabetes medications you take by mouth. (
  • A double-blind, randomized, placebo-controlled study was carried out on 44 hypertensive type 2 diabetic subjects previously treated by diet associated or not with sulfonylurea to assess the effects of acarbose -induced glycemic control on blood pressure (BP) and hormonal parameters . (
  • Acarbose monotherapy or combined with sulfonylurea was effective in improving glycemic control in hypertensive diabetic patients . (
  • Acarbose imitates the slowing of dietary carbohydrate digestion, suggesting that choosing a diet with a low glycemic index might be a potential strategy for reducing the negative metabolic effect of chronic exposure to benzene for smokers or people living/working in urban environments with high concentrations of exposure to automobile exhausts. (
  • Do not stop taking acarbose without talking to your doctor. (
  • Your doctor may want you to stop taking acarbose for a short time if any of these situations affect you. (
  • The antihyperglycemic action of acarbose results from a competitive, reversible inhibition of pancreatic alpha-amylase and membrane-bound intestinal alpha-glucoside hydrolase enzymes. (
  • However, it was difficult to identify that the effect on the incretins was due to the long-term improvement of glucotoxicity or the intrinsic action of acarbose. (
  • 1. Reactive hypoglycaemia due to late dumping syndrome: successful treatment with acarbose. (
  • 12. Long-term treatment with acarbose for the treatment of reactive hypoglycemia. (
  • 20. Treatment with acarbose in severe hypoglycaemia due to late dumping syndrome. (
  • If a patient using acarbose has a bout of hypoglycemia, the patient must eat something containing monosaccharides, such as glucose tablets or gel (GlucoBurst, Insta-Glucose, Glutose, Level One) and a doctor should be called. (
  • 6. Acarbose in reactive hypoglycemia: a double-blind study. (
  • 9. Post-prandial hypoglycemia after bariatric surgery: pharmacological treatment with verapamil and acarbose. (
  • Acarbose is an oral alpha-glucosidase inhibitor for use in the management of type 2 diabetes mellitus. (
  • Acarbose is an alpha glucosidase inhibitor which decreases intestinal absorption of carbohydrates and is used as an adjunctive therapy in the management of type 2 diabetes. (
  • Acarbose (ay' kar bose) is an inhibitor of intestinal alpha glucosidase, an enzyme responsible for digestion and absorption of starch, disaccharides and dextrin. (
  • Acarbose was approved for use in the United States in 1995 and was the first alpha glucosidase inhibitor introduced into clinical practice. (
  • Acarbose, an a-glucosidase inhibitor, controls postprandial hyperglycemia by slowing carbohydrate digestion and absorption. (
  • Acarbose, an α-glucosidase inhibitor, is a polysaccharide that could be used as a hypoglycemic drug since it slows down the intestinal absorption of carbohydrates [ 6 ]. (
  • BACKGROUND: The effect of the α-glucosidase inhibitor acarbose on cardiovascular outcomes in patients with coronary heart disease and impaired glucose tolerance is unknown. (
  • Thus CM is more effective alpha glucosidase inhibitor and at lower concentration than acarbose. (
  • Alpha glucosidase inhibitor, acarbose, is shown to control postprandial hyperglycemic shoot up [ 3 ] and is safe and well tolerated [ 4 ]. (
  • It is important that you and other members of your household understand this difference between acarbose and other medications used to treat diabetes. (
  • Acarbose (INN) is an anti-diabetic drug used to treat diabetes mellitus type 2 and, in some countries, prediabetes. (
  • However, a large study concluded in 2013 that "acarbose is effective, safe and well tolerated in a large cohort of Asian patients with type 2 diabetes. (
  • Acarbose qualifies as a first-line treatment for newly diagnosed patients with type 2 diabetes, for patients who have high postprandial blood glucose and for patients where dietary treatment alone provides inadequate glycaemic control. (
  • In patients with type 2 diabetes with fasting hyperglycaemia above 11.0 mmol/L, acarbose may be combined with other well-established anti-hyperglycaemic agents, resulting in an additional lowering of HbA 1c . (
  • Acarbose use is appropriate in elderly patients with type 2 diabetes, where asymptomatic hypoglycaemic reactions are potentially dangerous. (
  • As a consequence of plasma glucose reduction, acarbose reduces levels of glycosylated hemoglobin in patients with type 2 diabetes mellitus. (
  • As a consequence of plasma glucose reduction, Acarbose Tablets reduce levels of glycosylated hemoglobin in patients with type 2 diabetes mellitus. (
  • Chiasson JL, Josse RG, Gomis R, Hanefeld M, Karasik A, Laakso M. Acarbose for prevention of type 2 diabetes mellitus: the STOP-NIDDM randomised trial. (
  • Acarbose is used to treat type 2 diabetes. (
  • This study aimed to examine the effects of single-dose acarbose on the secretion of incretins in patients with newly diagnosed type 2 diabetes mellitus (T2DM). (
  • Effects of acarbose on cardiovascular and diabetes outcomes in patients with coronary heart disease and impaired glucose tolerance (ACE): a randomised, double-blind, placebo-controlled trial. (
  • We aimed to assess whether acarbose could reduce the frequency of cardiovascular events in Chinese patients with established coronary heart disease and impaired glucose tolerance, and whether the incidence of type 2 diabetes could be reduced. (
  • INTERPRETATION: In Chinese patients with coronary heart disease and impaired glucose tolerance, acarbose did not reduce the risk of major adverse cardiovascular events, but did reduce the incidence of diabetes. (
  • Additionally, feeding mice with Acarbose, a clinically available anti-diabetes drug, protected against benzene induced central and peripheral metabolic imbalance. (
  • Acarbose is a complex oligosaccharide that delays the digestion of ingested carbohydrates, thereby resulting in a smaller rise in blood glucose concentration following meals. (
  • Acarbose is a complex oligosaccharide produced in bacteria that has activity against glucoamylase, sucrase, maltase and isomaltase, intestinal brush border glucosidases. (
  • Acarbose works by slowing the action of certain chemicals that break down food to release glucose (sugar) into your blood. (
  • Acarbose is a starch blocker, and inhibits alpha glucosidase, an intestinal enzyme that releases glucose from larger carbohydrates. (
  • However the maximum dose per day is 600 mg.[citation needed] Since acarbose prevents the degradation of complex carbohydrates into glucose, some carbohydrate will remain in the intestine and be delivered to the colon. (
  • Acarbose is an oligosaccharide which is obtained from fermentation processes of a microorganism, Actinoplanes utahensis, and is chemically known as O-4,6-dideoxy- 4-[[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)-2-cyclohexen-1-yl]amino]-α-D-glucopyranosyl-(1 → 4)-O-α-D-glucopyranosyl-(1 → 4)-D-glucose. (
  • One metabolite (formed by cleavage of a glucose molecule from acarbose) also has alpha-glucosidase inhibitory activity. (
  • Alpha-glucosidase inhibitors (such as acarbose ) decrease the absorption of carbohydrates from the digestive tract, thereby lowering the after-meal glucose levels. (
  • Chinese patients with coronary heart disease and impaired glucose tolerance were randomly assigned (1:1), in blocks by site, by a centralised computer system to receive oral acarbose (50 mg three times a day) or matched placebo, which was added to standardised cardiovascular secondary prevention therapy. (
  • 3. Acarbose treatment of infant dumping syndrome: extensive study of glucose dynamics and long-term follow-up. (
  • Intestinal absorption studies using noneverted intestinal sacs, as well as in vivo studies in streptozotocin-induced diabetic rats using oral glucose tolerance with maltose and sucrose load, revealed better inhibition of alpha glucosidase as compared to acarbose. (
  • Since acarbose prevents the digestion of complex carbohydrates, the drug should be taken at the start of main meals (taken with first bite of meal). (
  • Acarbose slows the digestion of carbohydrates in the body, which helps control blood sugar levels. (
  • Acarbose inhibits enzymes (glycoside hydrolases) needed to digest carbohydrates, specifically, alpha-glucosidase enzymes in the brush border of the small intestines, and pancreatic alpha-amylase. (
  • Acarbose binds to the α-glycosidase and thus inhibits food polysaccharides or disaccharides from being decomposed into monosaccharide and subsequently absorbed into the bloodstream [ 6 ]. (
  • The delayed absorption of acarbose-related radioactivity reflects the absorption of metabolites that may be formed by either intestinal bacteria or intestinal enzymatic hydrolysis. (
  • Liver injury from acarbose is clearly idiosyncratic and may relate to an immunological reaction to the bacterially derived oligosaccharide molecule or to alterations in the microbiome and absorption of bacterial products. (
  • Acarbose slows down the intestinal absorption of carbohydrates, but its effects on the secretion of incretins are still poorly known. (
  • In vitro inhibitory effects of cyandin-3-rutinoside on pancreatic α-amylase and its combined effect with acarbose. (
  • Moreover, the amount of complex carbohydrates in the meal will determine the effectiveness of acarbose in decreasing postprandial hyperglycemia. (
  • Acarbose is metabolized exclusively within the gastrointestinal tract, principally by intestinal bacteria, but also by digestive enzymes. (
  • These enzymes can make it harder for your body to absorb acarbose. (
  • tell your doctor and pharmacist if you are allergic to acarbose or any other drugs. (
  • You may be more likely to have hyperglycemia (high blood sugar) if you are taking acarbose with other drugs that raise blood sugar. (
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  • Inhibitory effect of black tea and its combination with acarbose on small intestinal α-glucosidase activity. (
  • Single-dose acarbose could reduce the secretion of GIP and glucagon after a mixed meal in patients with newly diagnosed T2DM. (
  • Acarbose causes malabsorption and gastrointestinal side effects of flatulence, diarrhea and abdominal boating are not uncommon. (
  • atazanavir decreases effects of acarbose by pharmacodynamic antagonism. (
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  • Acarbose comes as a tablet to take by mouth. (
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  • The intrigue around acarbose stems from its dual function: it influences metabolic health and reshapes our gut microbiota. (
  • Acarbose -induced improvement in metabolic control may reduce BP in these patients . (
  • Acarbose protects from central and peripheral metabolic imbalance induced by benzene exposure. (
  • In a study of 6 healthy men, less than 2% of an oral dose of acarbose was absorbed as active drug, while approximately 35% of total radioactivity from a 14 C-labeled oral dose was absorbed. (
  • When acarbose was given intravenously, 89% of the dose was recovered in the urine as active drug within 48 hours. (
  • Acarbose has been linked to rare instances of clinically apparent acute liver injury. (
  • Subsequent to approval and with wide clinical use, however, at least a dozen instances of clinically apparent liver injury have been linked to acarbose use. (
  • Clinically significant dumping syndrome occurs in approximately 10% of patients after any type of gastric surgery and in up to 50% of patients after laparoscopic Roux-en-Y gastric bypass. (
  • Acarbose has no inhibitory activity against lactase and consequently would not be expected to induce lactose intolerance. (
  • alpha-Glucosidase inhibitory activity of cyanidin-3-galactoside and synergistic effect with acarbose. (
  • Kinetic studies using Lineweaver Burk plot showed mixed to noncompetitive type of inhibition by CM. In vivo studies with maltose load of 2 mg and 3 mg/gm body weight showed a noncompetitive pattern of inhibition at 5 mg/kg body weight of CM as against 60 mg/kg body weight of acarbose. (
  • This page shows results related to Acarbose and Thrombocytopenia from the FDA Adverse Event Reporting System (AERS). (
  • To learn more about all adverse events for Acarbose, view the complete Acarbose adverse event report . (
  • Acarbose tablets are available as 100 mg tablets for oral use. (
  • In addition, acarbose diminishes the insulinotropic and weight-increasing effects of sulfonylureas. (
  • 8. Postprandial hypoglycaemia after Roux-en-Y gastric bypass and the effects of acarbose, sitagliptin, verapamil, liraglutide and pasireotide. (
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  • Because acarbose blocks the breakdown of table sugar and other complex sugars, fruit juice or other products containing these sugars will not help to increase blood sugar. (
  • While you are taking acarbose, candy or table sugar (sucrose) may not work as well as dextrose in quickly raising your blood sugar. (
  • Acarbose is also degraded to maltose and acarviosin by the glucosidase cyclomaltodextrinase from gut bacteria Lactobacillus plantarum. (
  • In nature, acarbose is synthesized by soil bacteria Actinoplanes sp through its precursor valienamine. (
  • And acarbose is also degraded by gut bacteria Lactobacillus plantarum and soil bacteria Thermus sp by acarbose degrading glucosidases. (
  • METHODS: The Acarbose Cardiovascular Evaluation (ACE) trial was a randomised, double-blind, placebo-controlled, phase 4 trial, with patients recruited from 176 hospital outpatient clinics in China. (
  • Because acarbose acts locally within the gastrointestinal tract, this low systemic bioavailability of parent compound is therapeutically desired. (
  • Are the Longevity Benefits of Acarbose Rooted in Its Effect on the Gut Microbiota? (
  • 0.05) were decreased after receiving acarbose with a mixed meal, but GLP-1 levels and GLP-1 AUC did not change. (